Research workbench
Len K30T mutant: a domain flip as a result of a single amino acid substitution
Analyse Len K30T mutant: a domain flip as a result of a single amino acid substitution in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4LVE
- Type
- protein
- Length
- 227 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Len
- UniProt
- P01625
- Pockets
- 2 · best druggability 0.34
Structure
x-ray diffraction · 2 distinct chains · 3% helix, 51% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Len | protein | 114 | 3% helix, 51% strand | P01625 |
| B | Len | protein | 113 | 3% helix, 51% strand | P01625 |
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 80 | 0.34 | 0.75 | 21 | empty |
| 2 | 86 | 0.33 | 0.74 | 18 | empty |
Interfaces
1 interface between chains.
- A–B · 796 Ų buried · 7 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 4LVE · Len K30T mutant: a domain flip as a result of a single amino acid substitution · the same entry in another collection · chain A against A, TM-score 1.00
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt P01625
- Elsewhere: RCSB PDB 4LVE · PDBe 4LVE · UniProt P01625
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